Roles of plasma membrane-associated sialidase NEU3 in human cancers

Taeko Miyagi1, Tadashi Wada, Kazunori Yamaguchi

  • 1Biochemistry Division, Miyagi Cancer Center Research Institute, 47-1 Nodayama, Medeshima-shiode, Natori, Miyagi, 981-1293, Japan. miyagi-ta173@pref.miyagi.jp

Insights

Altered sialylation in cancer involves the enzyme sialidase NEU3, which is upregulated in many cancers. This enzyme promotes cancer malignancy and may serve as a diagnostic and therapeutic target.

Area of Science:

  • Biochemistry
  • Oncology
  • Molecular Biology

Background:

  • Altered sialylation of glycosphingolipids is a common cancer phenotype, affecting tumor antigens, cell adhesion, and signaling.
  • Sialidases, enzymes that remove sialic acids, are crucial for understanding these alterations.

Purpose of the Study:

  • To investigate the pathological significance of aberrant ganglioside alterations in cancer.
  • To focus on the role of sialidase NEU3 in cancer development and progression.

Main Methods:

  • Focus on the human sialidase NEU3, noting its plasma membrane localization and specific hydrolysis of gangliosides.
  • Summarize recent findings on sialidase alterations and their implications in cancer.

Main Results:

  • Sialidase NEU3 is significantly upregulated in various cancers, including colon and renal carcinomas.
  • NEU3 suppresses apoptosis in cancer cells, contributing to malignancy.
  • NEU3 is closely linked to cancer malignancy.

Conclusions:

  • Sialidase NEU3 plays a critical role in cancer progression.
  • NEU3 represents a potential target for cancer diagnosis and therapy.

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